Inactivates vasopressin and oxytocin by splitting off glycinamide. Also cleaves ester substrates of trypsin and chymotrypsin. Although glycinamide is by far the preferred leaving group, other aminoacylamides may also be released, e.g. phenylalaninamide. The toad skin enzyme is inhibited by diisopropyl fluorophosphate.
Fruhaufová, L., Suska-Brezezinska, E., Barth, T. and Rychlik, I. Rat liver enzyme inactivating oxytocin and its deamino-carba analogues. Coll. Czech. Chem. Commun.38 (1973) 2793–2798.
Nardacci, N.J., Mukhopadhyay, S. and Campbell, B.J. Partial purification and characterization of the antidiuretic hormone in toad bladder. Biochim. Biophys. Acta377 (1975) 146–157. [DOI] [PMID: 1122284]
Simmons, W.H. and Walter, R. Carboxamidopeptidase: purificaction and characterization of a neurohypophyseal hormone inactivating peptidase from toad skin. Biochemistry19 (1980) 39–48. [PMID: 6766314]
[EC 188.8.131.52 created 1978 as EC 184.108.40.206, transferred 1981 to EC 220.127.116.11]